Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00883

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Oryctolagus cuniculus
UNIPROT: P00883


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


The taxonomic range for the selected organisms is: Oryctolagus cuniculus

EC NUMBER
COMMENTARY hide
4.1.2.13
-
RECOMMENDED NAME
GeneOntology No.
fructose-bisphosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde assimilation III (dihydroxyacetone cycle)
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gluconeogenesis III
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glycolysis III (from glucose)
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glycolysis V (Pyrococcus)
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gluconeogenesis II (Methanobacterium thermoautotrophicum)
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glycolysis IV (plant cytosol)
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formaldehyde assimilation II (assimilatory RuMP Cycle)
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sucrose biosynthesis I (from photosynthesis)
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Calvin-Benson-Bassham cycle
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glycolysis I (from glucose 6-phosphate)
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gluconeogenesis I
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1,3-propanediol biosynthesis (engineered)
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sucrose degradation V (sucrose alpha-glucosidase)
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glycolysis II (from fructose 6-phosphate)
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glycolysis
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photosynthesis
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Glycolysis / Gluconeogenesis
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Pentose phosphate pathway
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Fructose and mannose metabolism
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Methane metabolism
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Carbon fixation in photosynthetic organisms
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-52-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
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-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
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r
2 acetaldehyde
5-deoxy-D-threo-2-pentulose
show the reaction diagram
-
-
yield 29%
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?
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
show the reaction diagram
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yield 38%
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?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
show the reaction diagram
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yield 13%
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?
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
show the reaction diagram
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yield 34%
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?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
dihydroxyacetone phosphate
?
show the reaction diagram
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-
-
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?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
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-
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sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
show the reaction diagram
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-
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?
additional information
?
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the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
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r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
additional information
?
-
-
the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucitol 1,6-bisphosphate
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competitive inhibitor
D-mannitol 1,6-bisphosphate
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competitive inhibitor
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
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fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
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fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
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fructose-1,6-bisphosphate analogue
phosphoglycoloamidoxime
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dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
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dihydroxyacetone phosphate analogue
(NH4)2SO4
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50% inhibition at 6.2 mM at 37C, 50% inhibition at 5.27 mM at 5C
1-hydroxy-2-naphthaldehyde 6-phosphate
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slow-binding
2,4-Dihydroxybenzaldehyde 4-phosphate
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2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
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2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
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2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
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2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
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3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
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4-Hydroxybenzaldehyde phosphate
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competitive
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4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
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5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
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1 mM, 15 min incubation time, 80% residual activity
ADP
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50% inhibition at 2.7 mM at 37C, 50% inhibition at 5.4 mM at 5C
AMP
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50% inhibition at 4.5 mM at 37C, 50% inhibition at 6.0 mM at 5C
ATP
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50% inhibition at 2.1 mM at 37C, 50% inhibition at 2.1 mM at 5C
citrate
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50% inhibition at 2.7 mM at 37C, 50% inhibition at 3.4 mM at 5C
CuSO4
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0.02 mM, inactivation
D-erythrulose 1-phosphate
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slow reversible
Hydroquinone diphosphate
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competitive
IMP
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50% inhibition at 4.2 mM at 37C, 50% inhibition at 8.5 mM at 5C
KCl
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50% inhibition at 111 mM at 37C, 50% inhibition at 63.3 mM at 5C
Magnesium citrate
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50% inhibition at 9 mM at 37C, 50% inhibition at 2.5 mM at 5C
mannitol-1,6-bis(phosphate)
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competitive
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
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NaBH4
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irreversible inactivation
NaCl
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50% inhibition at 110 mM at 37C, 50% inhibition at 52 mM at 5C
naphthyl 2,6-bisphosphate
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competitive
NH4Cl
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50% inhibition at 166 mM at 37C, 50% inhibition at 40.6 mM at 5C
o-phenanthroline
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0.06 mM, inactivation
peroxynitrite
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decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity
phosphate
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50% inhibition at 6.1 mM at 37C, 50% inhibition at 1.7 mM at 5C
phosphatidylserine
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phosphoglycolo hydroxamic acid
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PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
pyridoxal 5'-phosphate
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Resorcinol diphosphate
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competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
D-fructose 1,6-bisphosphate
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0.055
D-fructose-1,6-bisphosphate
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0.00084 - 13.4
D-fructose 1,6-bisphosphate
0.723 - 40
D-Fructose 1-phosphate
0.8 - 11
fructose 1-phosphate
0.3 - 1
glyceraldehyde 3-phosphate
0.4 - 2
glycerone phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 42.2
D-fructose 1,6-bisphosphate
0.63 - 6.08
D-Fructose 1-phosphate
0.167 - 0.267
fructose 1-phosphate
additional information
additional information
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turnover-numbers of wild-type and mutant enzymes
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
D-glucitol 1,6-bisphosphate
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0.0073
D-mannitol 1,6-bisphosphate
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0.125
1-hydroxy-2-naphthaldehyde 6-phosphate
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wild-type enzyme
0.067
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
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in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.37
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
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2.5
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
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in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.4
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
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in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.264
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
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in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.85
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
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in glycyl-glycine buffer (0.1 M pH 7.4), temperature not specified in the publication
0.001
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
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-
0.00028 - 0.013
naphthyl 2,6-bisphosphate
0.001
phosphoglycolo hydroxamic acid
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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E187A and E189Q mutant
8
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broad optimum, wild-type and E189A mutant
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.1
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pH 5.5: 58% of maximal activity, pH 9.1: 85% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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FBPasealdolase complex is located on an actinin of the Z-line. The stability of the complex is regulated by calcium ions. Elevated calcium concentration decreases association constant of FBPasealdolase and FBPase-alpha-actinin complex, causes fast dissociation of FBPase from the Z-line and slow accumulation of aldolase within the I-band and M-line. Release of Ca2+ during muscle contraction might result, simultaneously, in the inhibition of glyconeogenesis and in the acceleration of glycolysis
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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SDS-PAGE
41000
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4 * 41000, SDS-PAGE
142000 - 160000
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ultracentrifugation experiments
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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rabbit muscle D128V aldolase. The D128V mutation causes aldolase to lose intermolecular contacts with the neighbouring subunit at one of the two interfaces of the tetramer
tetramer
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wild-type
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method
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complexed with fructose 1,6-bisphosphate
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D33N and D33S mutant enzymes
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in complex with dihydroxyacetone phosphate
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recombinant enzyme, vapour diffusion method. Crystal structures are determined to 1.8 resolution of fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex corresponds to the postulated Schiff base intermediate and has reaction geometry consistent with incipient C3-C4 bond cleavage catalyzed by Glu187, which is adjacent to the Schiff base-forming Lys229
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vapor diffusion method and/or batch crystallization
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
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80% loss of activity, irreversible
4910
10
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30C, 15 min, 5% loss of activity
4910
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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pH 10, 15 min, 5% loss of activity
37
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native enzyme is completely stable
50
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pH 7.0, 10 min, stable up to
60
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pH 7.0, 10 min, about 15% loss of activity with D-fructose 1,6-bisphosphate
80
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pH 7.0, 10 min, about 35% loss of activity with D-fructose 1,6-bisphosphate
90
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pH 7.0, 10 min, complete loss of activity with D-fructose 1,6-bisphosphate
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose CL-6B chromatography
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phenyl-Sepharose column chromatography and hydroxylapatite chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21 SI cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D128V
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mutation, mimicking the clinically important D128G mutation in humans
D33N
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the mutation drastically reduces the rate of turnover but does not impact substrate binding
D33S
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the mutation drastically reduces the rate of turnover but does not impact substrate binding
E189A
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almost no loss in catalytic activity
E189Q
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only small loss in catalytic activity
H156E
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similar kinetics and stability as wild-type enzyme
K229A
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K107M, K146M, K229M, K229A and E187Q, have decreased cleavage activity towards D-fructose 1,6-bisphosphate
S271
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mutation decreases by 1 order of magnitude the affinity of 1-hydroxy-2-naphthaldehyde 6-phosphate for the aldolase active site but does not modify its ability to catalyze Schiff base formation
additional information
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AB_All mutant, isozyme-specific residues from aldolase B swapped into aldolase A and vice versa, decreased Km and kcat compared to aldolase A, similar Km and kcat to aldolase B
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
renaturation of acid-denatured enzyme
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